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Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial (LTA3), Recombinant Protein
Cat: RP01955
Species: Arabidopsis thaliana (Mouse-ear cress)
Datasheet:
Product Info
Full Product Name
Recombinant Arabidopsis thaliana Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial (LTA3) , partial
Product Gene Name
LTA3 recombinant protein
Product Synonym Gene Name
LTA3
Purity
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Molecular Weight
68,862 Da
Storage
Store at -20℃. For long-term storage, store at -20℃ or -80℃. Store working aliquots at 4℃ for up to one week. Repeated freezing and thawing is not recommended.
Protein Family
Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex
NCBI/Uniprot Data
NCBI Accession #
NP_190788.1
NCBI GI #
15231159
NCBI GenBank Nucleotide #
NM_115080.3
NCBI GeneID
824385
NCBI Official Full Name
Dihydrolipoamide acetyltransferase, long form protein
NCBI Official Symbol
LTA3
NCBI Official Synonym Symbols
DIHYDROLIPOAMIDE S-ACETYLTRANSFERASE
NCBI Protein Information
Dihydrolipoamide acetyltransferase, long form protein
NCBI Summary
dihydrolipoamide S-acetyltransferase (LTA3) mRNA, nuclear
UniProt Gene Name
LTA3
UniProt Synonym Gene Names
PDC-E2 1; PDCE2 1
UniProt Protein Name
Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
UniProt Synonym Protein Names
Dihydrolipoamide S-acetyltransferase component 1 of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2 1; PDC-E2 1; PDCE2 1
UniProt Primary Accession #
Q0WQF7
UniProt Secondary Accession #
Q39082; Q9SQI7; Q9SUY5
UniProt Related Accession #
Q0WQF7
UniProt Comments
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
For research use only, not for clinical use.